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  Dual-fluorescence L-amino acid reports insertion and orientation of melittin peptide in cell membranes.

Postupalenko, V. Y., Zamotaiev, O. M., Shvadchak, V. V., Strizhak, A. V., Pivovarenko, V. G., Klymchenko, A. S., et al. (2013). Dual-fluorescence L-amino acid reports insertion and orientation of melittin peptide in cell membranes. Bioconjugate Chemistry, 24(12), 1998-2007. doi:10.1021/bc400325n.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-0E86-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-358B-2
Genre: Journal Article

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http://pubs.acs.org/doi/pdf/10.1021/bc400325n (Publisher version)
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Postupalenko, V. Y., Author
Zamotaiev, O. M., Author
Shvadchak, V. V.1, Author              
Strizhak, A. V., Author
Pivovarenko, V. G., Author
Klymchenko, A. S., Author
Mely, Y., Author
Affiliations:
1Department of Laboratory of Cellular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578628              

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 Abstract: Monitoring insertion and orientation of peptides in situ on cell membranes remains a challenge. To this end, we synthesized an l-amino acid (AFaa) containing a dual-fluorescence dye of the 3-hydroxyflavone family, as a side chain. In contrast to other labeling approaches using a flexible linker, the AFaa fluorophore, introduced by solid phase synthesis into desired position of a peptide, is attached closely to its backbone with well-defined orientation, and, therefore, could reflect its localization in the membrane. This concept was validated by replacing the leucine-9 (L9) and tryptophan-19 (W19) residues by AFaa in melittin, a well-studied membrane-active peptide. Due to high sensitivity of AFaa dual emission to the environment polarity, we detected a much deeper insertion of L9 peptide position into the bilayer, compared to the W19 position. Moreover, using fluorescence microscopy with a polarized light excitation, we found different orientation of AFaa at L9 and W19 positions of melittin in the bilayers of giant vesicles and cellular membranes. These results suggested that in the natural membranes, similarly to the model lipid bilayers, melittin is preferentially oriented parallel to the membrane surface. The developed amino acid and the proposed methodology will be of interest to study other membrane peptides.

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Language(s): eng - English
 Dates: 2013-11-242013-12
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/bc400325n
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Title: Bioconjugate Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 24 (12) Sequence Number: - Start / End Page: 1998 - 2007 Identifier: ISSN: 1043-1802